SPN3_SCHPO
ID SPN3_SCHPO Reviewed; 412 AA.
AC P48008; Q9HGN0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Septin homolog spn3;
GN Name=spn3; ORFNames=SPBC16A3.01, SPBC543.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Al-Awar O.S., Pugh T.A., Kim H.B., Valencik M.L., Pringle J.R.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Al-Awar O.S.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEPTIN COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15385632; DOI=10.1091/mbc.e04-07-0640;
RA An H., Morrell J.L., Jennings J.L., Link A.J., Gould K.L.;
RT "Requirements of fission yeast septins for complex formation, localization,
RT and function.";
RL Mol. Biol. Cell 15:5551-5564(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Plays a role in the cell cycle. Involved in a late stage of
CC septum formation leading to the separation of the daughter cells.
CC {ECO:0000269|PubMed:15385632}.
CC -!- SUBUNIT: Component of the septin complex composed of two copies of each
CC spn1, spn2, spn3 and spn4. {ECO:0000269|PubMed:15385632}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15385632}. Note=Localizes to the medial ring at the
CC cell cortex of dividing cells.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; U29889; AAB53691.2; -; mRNA.
DR EMBL; CU329671; CAA16852.1; -; Genomic_DNA.
DR PIR; T52561; T52561.
DR RefSeq; XP_001713152.1; XM_001713100.2.
DR AlphaFoldDB; P48008; -.
DR SMR; P48008; -.
DR BioGRID; 276573; 41.
DR STRING; 4896.SPBC16A3.01.1; -.
DR iPTMnet; P48008; -.
DR MaxQB; P48008; -.
DR PaxDb; P48008; -.
DR PRIDE; P48008; -.
DR EnsemblFungi; SPBC16A3.01.1; SPBC16A3.01.1:pep; SPBC16A3.01.
DR PomBase; SPBC16A3.01; spn3.
DR VEuPathDB; FungiDB:SPBC16A3.01; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; P48008; -.
DR OMA; VNCEDSW; -.
DR PhylomeDB; P48008; -.
DR Reactome; R-SPO-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SPO-111469; SMAC, XIAP-regulated apoptotic response.
DR PRO; PR:P48008; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0032151; C:mitotic septin complex; IDA:PomBase.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IMP:PomBase.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; GTP-binding; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..412
FT /note="Septin homolog spn3"
FT /id="PRO_0000173505"
FT DOMAIN 49..325
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 59..66
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 118..121
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 200..203
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 350..396
FT /evidence="ECO:0000255"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 201..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 412 AA; 46661 MW; 15949D31A1B7B316 CRC64;
MWYTYNEDFG VVQLLFLHSN DTLTARTHIT KGQIDIELTM RTTKKSSKKG IPLNLMVVGD
VGLGRTAFIN TLCEKPLIRH NNNFDPAEAS SVSPVEIVPY QTDIILEDGT KINLTVLDTP
HFGEAIDNEN NFDIILQYIE SQYDNVLEEE SRIKRNARFC DDRVHALIYF ISPTGHGLRE
LDIELMRRLA PRVNIIPAIA KADSLTAQEL QTTKEMINAD IEYYKIPVYD FPYDIEEDEE
AIINLSQQLR ATIPFAIVSS DRLIEMNGQT VRGRAYPWGV VEVDNPRHSD FLALRSALFA
THIEDLHNIT SNQLYETYRT EKLSTSQLLL DSTVGLDGKN LSQHDQVLRE DRLRAIELSV
QKEIEEKRRQ LLAREEALRA LEEKLAASTA AMANASVSTL PSSVSSTNHS QS
